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4D5M

Gonadotropin-releasing hormone agonist

Summary for 4D5M
Entry DOI10.2210/pdb4d5m/pdb
DescriptorTRIPTORELIN, PHOSPHATE ION (3 entities in total)
Functional Keywordshormone, gnrh, lhrh, d-trp, decapeptide
Biological sourceSYNTHETIC CONSTRUCT
Total number of polymer chains4
Total formula weight5534.75
Authors
Legrand, P.,Le Du, M.-H.,Valery, C.,Deville-Foillard, S.,Paternostre, M.,Artzner, F. (deposition date: 2014-11-05, release date: 2015-08-12, Last modification date: 2024-10-16)
Primary citationValery, C.,Deville-Foillard, S.,Lefebvre, C.,Taberner, N.,Legrand, P.,Meneau, F.,Meriadec, C.,Delvaux, C.,Bizien, T.,Kasotakis, E.,Lopez-Iglesias, C.,Gall, A.,Bressanelli, S.,Le Du, M.-H.,Paternostre, M.,Artzner, F.
Atomic View of the Histidine Environment Stabilizing Higher- Ph Conformations of Ph-Dependent Proteins.
Nat.Commun., 6:7771-, 2015
Cited by
PubMed Abstract: External stimuli are powerful tools that naturally control protein assemblies and functions. For example, during viral entry and exit changes in pH are known to trigger large protein conformational changes. However, the molecular features stabilizing the higher pH structures remain unclear. Here we elucidate the conformational change of a self-assembling peptide that forms either small or large nanotubes dependent on the pH. The sub-angstrom high-pH peptide structure reveals a globular conformation stabilized through a strong histidine-serine H-bond and a tight histidine-aromatic packing. Lowering the pH induces histidine protonation, disrupts these interactions and triggers a large change to an extended β-sheet-based conformation. Re-visiting available structures of proteins with pH-dependent conformations reveals both histidine-containing aromatic pockets and histidine-serine proximity as key motifs in higher pH structures. The mechanism discovered in this study may thus be generally used by pH-dependent proteins and opens new prospects in the field of nanomaterials.
PubMed: 26190377
DOI: 10.1038/NCOMMS8771
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (0.85 Å)
Structure validation

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